Building β-peptide H10/12 foldamer helices with six-membered cyclic side-chains: fine-tuning of folding and self-assembly

István M Mándity; Livia Fülöp; Elemér Vass; Gábor K Tóth; Tamás A Martinek; Ferenc Fülöp

doi:10.1021/ol102494m

Building β-peptide H10/12 foldamer helices with six-membered cyclic side-chains: fine-tuning of folding and self-assembly

Org Lett. 2010 Dec 3;12(23):5584-7. doi: 10.1021/ol102494m. Epub 2010 Nov 4.

Authors

István M Mándity¹, Livia Fülöp, Elemér Vass, Gábor K Tóth, Tamás A Martinek, Ferenc Fülöp

Affiliation

¹ Institute of Pharmaceutical Chemistry, University of Szeged, H-6720 Szeged, Eötvös u. 6, Hungary.

PMID: 21050013
DOI: 10.1021/ol102494m

Abstract

The ability of the β-peptidic H10/12 helix to tolerate side-chains containing six-membered alicyclic rings was studied. cis-2-Aminocyclohex-3-ene carboxylic acid (cis-ACHEC) residues afforded H10/12 helix formation with alternating backbone configuration. Conformational polymorphism was observed for the alternating cis-ACHC hexamer, where chemical exchange takes place between the major left-handed H10/12 helix and a minor folded conformation. The hydrophobically driven self-assembly was achieved for the cis-ACHC-containing helix which was observed as vesicles ~100 nm in diameter.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cyclization
Hydrophobic and Hydrophilic Interactions
Microscopy, Electron, Transmission
Models, Molecular
Peptides / chemistry*
Protein Folding*
Protein Structure, Secondary

Substances

Peptides